Literature summary for 1.17.4.1 extracted from

Cerqueira, N.M.; Fernandes, P.A.; Ramos, M.J.
Ribonucleotide reductase: a critical enzyme for cancer chemotherapy and antiviral agents (2007), Recent Pat. Anticancer Drug Discov., 2, 11-29.

Search for more literature for 1.17.4.1

Inhibitors

Inhibitors	Comment	Organism	Structure
(E)-2'-fluoromethylene-2'-deoxycytidine-5-diphosphate	i.e. N3dNDP, inhibitor forming a furanone intermediate. Modeling of enzyme-inhibitor complex	Escherichia coli
gemcitabine	i.e. F2dNDP, inhibitor forming a furanone intermediate. Modeling of enzyme-inhibitor complex	Escherichia coli
additional information	reaction involves formation of a keto-deoxyribonucleotide intermediate. In case of furanone inhibitors, the intermediate dissociates from the active site, depending on the solvation free energy of the 2-substituents, its influence inside the active site, and the charge transfer mechanism from a protein side chain to solution as thermodynamic driving forces. Substrates do not dissociate from the active site but complete the catalytic cycle	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	use of crystal structure for modeling of active site	-

Reaction

Reaction	Comment	Organism	Reaction ID
2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin	reaction involves formation of a keto-deoxyribonucleotide intermediate. In case of furanone inhibitors, the intermediate dissociates from the active site, depending on the solvation free energy of the 2-substituents, its influence inside the active site, and the charge transfer mechanism from a protein side chain to solution as thermodynamic driving forces. Substrates do not dissociate from the active site but complete the catalytic cycle	Escherichia coli	a

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)